Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

Genes and Development

Volumn 19, Issue 12, 2005, Pages 1455-1465

  Couture, Jean François ^a   Collazo, Evys ^a   Brunzelle, Joseph S ^b   Trievel, Raymond C ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

Histone modifications; Mitosis; Protein lysine methylation; SET domain; Substrate specificity; Transcription

Indexed keywords

ENZYME SET8; HISTONE H4; METHYLTRANSFERASE; S ADENOSYLHOMOCYSTEINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CELL DIVISION; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROGEN BOND; HYDROPHOBICITY; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN METHYLATION; STRUCTURE ANALYSIS;

BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; S-ADENOSYLHOMOCYSTEINE; SUBSTRATE SPECIFICITY;

METAZOA;

EID: 22344454519     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1318405     Document Type: Article

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